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SYSTEMATIC NAME

IUBMB Comments

2,3-diketo-5-methylthiopentyl-1-phosphate keto-enol-isomerase

The enzyme participates in the methionine salvage pathway in Bacillus subtilis [2].
In some species a single bifunctional enzyme, EC 3.1.3.77, acireductone synthase, catalyses both this reaction and EC 3.1.3.87, 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase [1].

the enzyme belongs to the RuBisCO superfamily. The functionally divergent Geobacillus kaustophilus member of the RuBisCO superfamily uses the same structural strategy as RuBisCO for stabilizing the enolate anion intermediate, i.e., coordination to an essential Mg2+, but the proton abstraction is catalyzed by a different general base

the enzyme belongs to the RuBisCO superfamily. The functionally divergent Geobacillus kaustophilus member of the RuBisCO superfamily uses the same structural strategy as RuBisCO for stabilizing the enolate anion intermediate, i.e., coordination to an essential Mg2+, but the proton abstraction is catalyzed by a different general base

phylogenetic tree of RuBisCO and RLPs, overview. The RLP of Bacillus subtilis includes both those amino acid residues of RuBisCO that are responsible for binding the phosphate on C1 of RuBP and those required for activation by CO2. However, the residues of RuBisCO that are responsible for binding the other phosphate group of RuBP and the residues of loop 6, which are essential for RuBisCO activity are replaced by different amino acids in RLP

the enzyme belongs to the RubisCO-like protein, RLP, family of proteins. Unlike Bacillus subtilis RLP, Rodospirillum rubrum RLP does not catalyze the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate. Instead, under aerobic growth conditions, R. rubrum RLP employs another intermediate of the MSP, 5-methylthioribulose-1-phosphate, as a substrate, resulting in the formation of different products

members of the form IV subfamily, Rubisco-like proteins or RLPs, do not display Rubisco activity, but the two eubacterial members of this family play a role in sulfur metabolism. Discovery of the coexistence of RbcLI and RbcLIV in cyanobacteria, the ancestors of chloroplasts, enlightens episodes of the chaotic evolutionary history of the Rubiscos, a protein family of major importance for life on earth

the enzyme belongs to the RuBisCO superfamily. The functionally divergent Geobacillus kaustophilus member of the RuBisCO superfamily uses the same structural strategy as RuBisCO for stabilizing the enolate anion intermediate, i.e., coordination to an essential Mg2+, but the proton abstraction is catalyzed by a different general base

a growth-defective mutant, in which the gene for this RLP is disrupted, is rescued by the gene for RuBisCO from the photosynthetic bacterium Rhodospirillum rubrum, the photosynthetic RuBisCO from Rhodospirillum rubrum retains the ability to function in the methionine salvage pathway in Bacillus subtilis

the rlpA disruption strain of Rhodospirillum rubrum was incapable of using 5-methylthioadenosine as the sole sulfur source under aerobic growth conditions; the RLP disruption strain of Rhodospirillum rubrum is incapable of 5-methylthioadenosine-dependent growth under aerobic growth conditions. The rlpA disruption strain of Rhodospirillum rubrum is incapable of using 5-methylthioadenosine as the sole sulfur source under aerobic growth conditions

Klebsiella pneumoniae converts 2,3-diketo-5-methylthio-l-phosphopentane to formate, 2-keto-4-methylthiobutyrate, and 3-methylthiopropionate. 2,3-diketo-1-phosphohexane, the desthio analogue of the naturally occurring diketone, can serve as alternate substrate in the methionine salvage pathway

the enzyme is involved in the methionine salvage pathway. It is a heterofunctional homologue of RuBisCO catalyzing the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine

the enzyme is involved in the methionine salvage pathway. It is a heterofunctional homologue of RuBisCO catalyzing the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine

Rhodopseudomonas palustris RLP is involved in the methionine salvage pathway, it utilizes the methionine salvage pathway because it can grow using 5-methyladenosine as the sole source of sulfur, although the reaction step of DK-MTP-1-P enolase may be catalysed by a photosynthetic form II RuBisCO and not by RLPs, overview

Rhodospirillum rubrum RLP is involved in the methionine salvage pathway, it utilizes the methionine salvage pathway because it can grow using 5-methyladenosine as the sole source of sulfur, although the reaction step of DK-MTP-1-P enolase may be catalysed by a photosynthetic form II RuBisCO and not by RLPs, overview

the enzyme is involved in the methionine salvage pathway. It is a heterofunctional homologue of RuBisCO catalyzing the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine

Klebsiella pneumoniae converts 2,3-diketo-5-methylthio-l-phosphopentane to formate, 2-keto-4-methylthiobutyrate, and 3-methylthiopropionate. 2,3-diketo-1-phosphohexane, the desthio analogue of the naturally occurring diketone, can serve as alternate substrate in the methionine salvage pathway

Bacillus subtilis RLP catalyses an analogous reaction to photosynthetic RuBisCO since its substrate resembles the structure of RuBP, rationalizing the tight linkage between RLPs and RuBisCO. But Bacillus subtilis RLP functions as an enzyme in a different metabolic pathway from that of RuBisCO, overview

RLP is required for metabolizing 5-methylthioadenosine; RubisCO-like protein, RLP, is required for metabolizing 5-methylthioadenosine.the form II RubisCO enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions

RLP is required for metabolizing 5-methylthioadenosine; RubisCO-like protein, RLP, is required for metabolizing 5-methylthioadenosine.the form II RubisCO enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions

structure-function relationship, the active site KDDE motif with the carboxylated Lys173 as well as two carboxylate ligands Asp175 and Glu176 are essential for Mg2+ stabilization and also for stabilizing the enediolate intermediate, the carbamate group of the carboxylated Lys173 is the third ligand for the essential Mg2+ as well as the general base Lys98 that initiates the reaction by abstraction of the proton from the substrate

structure-function relationship, the active site KDDE motif with the carboxylated Lys173 as well as two carboxylate ligands Asp175 and Glu176 are essential for Mg2+ stabilization and also for stabilizing the enediolate intermediate, the carbamate group of the carboxylated Lys173 is the third ligand for the essential Mg2+ as well as the general base Lys98 that initiates the reaction by abstraction of the proton from the substrate

structure-function relationship, the active site KDDE motif with the carboxylated Lys173 as well as two carboxylate ligands Asp175 and Glu176 are essential for Mg2+ stabilization and also for stabilizing the enediolate intermediate, the carbamate group of the carboxylated Lys173 is the third ligand for the essential Mg2+ as well as the general base Lys98 that initiates the reaction by abstraction of the proton from the substrate

the enzyme catalyzes the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine. The reaction is accomplished by abstraction of the 1-proS proton from C1 of the DK-MTP 1-P substrate to form the tautomerized product, a conjugated enol. Stabilization of an enolate anion intermediate by coordination to an active site Mg2+. Structure-function relationships, overview. The enolase from Geobacillus kaustophilus catalyzes stereospecific abstraction of the 1-proS proton of the DK-MTP 1-P substrate

the enzyme catalyzes the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine. The reaction is accomplished by abstraction of the 1-proS proton from C1 of the DK-MTP 1-P substrate to form the tautomerized product, a conjugated enol. Stabilization of an enolate anion intermediate by coordination to an active site Mg2+. Structure-function relationships, overview. The enolase from Geobacillus kaustophilus catalyzes stereospecific abstraction of the 1-proS proton of the DK-MTP 1-P substrate

the enzyme catalyzes the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine. The reaction is accomplished by abstraction of the 1-proS proton from C1 of the DK-MTP 1-P substrate to form the tautomerized product, a conjugated enol. Stabilization of an enolate anion intermediate by coordination to an active site Mg2+. Structure-function relationships, overview. The enolase from Geobacillus kaustophilus catalyzes stereospecific abstraction of the 1-proS proton of the DK-MTP 1-P substrate

the form II RubisCO enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions

the form II RubisCO enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions

the enzyme catalyzes the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine. The reaction is accomplished by abstraction of the 1-proS proton from C1 of the DK-MTP 1-P substrate to form the tautomerized product, a conjugated enol. Stabilization of an enolate anion intermediate by coordination to an active site Mg2+. Structure-function relationships, overview. The enolase from Geobacillus kaustophilus catalyzes stereospecific abstraction of the 1-proS proton of the DK-MTP 1-P substrate

the enzyme catalyzes the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine. The reaction is accomplished by abstraction of the 1-proS proton from C1 of the DK-MTP 1-P substrate to form the tautomerized product, a conjugated enol. Stabilization of an enolate anion intermediate by coordination to an active site Mg2+. Structure-function relationships, overview. The enolase from Geobacillus kaustophilus catalyzes stereospecific abstraction of the 1-proS proton of the DK-MTP 1-P substrate

the enzyme catalyzes the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate in the methionine salvage pathway in which 5-methylthio-D-ribose derived from 5'-methylthioadenosine is converted to methionine. The reaction is accomplished by abstraction of the 1-proS proton from C1 of the DK-MTP 1-P substrate to form the tautomerized product, a conjugated enol. Stabilization of an enolate anion intermediate by coordination to an active site Mg2+. Structure-function relationships, overview. The enolase from Geobacillus kaustophilus catalyzes stereospecific abstraction of the 1-proS proton of the DK-MTP 1-P substrate

the form II RubisCO enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions

the form II RubisCO enzyme from the nonsulfur purple bacterium Rhodospirillum rubrum is also able to function as an enolase in vivo as part of an methionine salvage pathway, but only under anaerobic conditions

structure of the apo decarbamylated enzyme E form, computational structure analysis and modeling, structure comparison, overview. In the E form of DK-MTP-1P enolase the loop at 299-311, equivalent to loop-6 in RuBisCO, is in a closed conformation and the loop at 37-46, equivalent to the 60s loop, is positioned about 15 A away from the active site